CO6A1_CHICK
ID CO6A1_CHICK Reviewed; 1019 AA.
AC P20785;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Collagen alpha-1(VI) chain;
DE Flags: Precursor;
GN Name=COL6A1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1572359; DOI=10.1111/j.1432-1033.1992.tb16816.x;
RA Walchli C., Koller E., Trueb J., Trueb B.;
RT "Structural comparison of the chicken genes for alpha 1(VI) and alpha 2(VI)
RT collagen.";
RL Eur. J. Biochem. 205:583-589(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2784434; DOI=10.1016/s0021-9258(18)83585-2;
RA Bonaldo P., Russo V., Bucciotti F., Bressan G.M., Colombatti A.;
RT "Alpha 1 chain of chick type VI collagen. The complete cDNA sequence
RT reveals a hybrid molecule made of one short collagen and three von
RT Willebrand factor type A-like domains.";
RL J. Biol. Chem. 264:5575-5580(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RX PubMed=1396681; DOI=10.1111/j.1432-1033.1992.tb17246.x;
RA Koller E., Trueb B.;
RT "Characterization of the chicken alpha 1(VI) collagen promoter.";
RL Eur. J. Biochem. 208:769-774(1992).
CC -!- FUNCTION: Collagen VI acts as a cell-binding protein.
CC -!- SUBUNIT: Trimers composed of three different chains: alpha 1(VI), alpha
CC 2(VI), and alpha 3(VI).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
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DR EMBL; X64458; CAA45788.1; -; Genomic_DNA.
DR EMBL; X57998; CAA41062.1; -; Genomic_DNA.
DR EMBL; J04598; AAB59954.1; -; mRNA.
DR EMBL; X57987; CAA41053.1; -; Genomic_DNA.
DR PIR; A32856; A32856.
DR RefSeq; NP_990438.1; NM_205107.1.
DR AlphaFoldDB; P20785; -.
DR SMR; P20785; -.
DR STRING; 9031.ENSGALP00000038878; -.
DR PaxDb; P20785; -.
DR GeneID; 396000; -.
DR KEGG; gga:396000; -.
DR CTD; 1291; -.
DR VEuPathDB; HostDB:geneid_396000; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P20785; -.
DR OrthoDB; 140989at2759; -.
DR PhylomeDB; P20785; -.
DR PRO; PR:P20785; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005594; C:collagen type IX trimer; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0008585; P:female gonad development; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF00092; VWA; 3.
DR SMART; SM00327; VWA; 3.
DR SUPFAM; SSF53300; SSF53300; 3.
DR PROSITE; PS50234; VWFA; 3.
PE 2: Evidence at transcript level;
KW Cell adhesion; Collagen; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..1019
FT /note="Collagen alpha-1(VI) chain"
FT /id="PRO_0000005760"
FT DOMAIN 37..233
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 613..800
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 824..1012
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 248..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 476..478
FT /note="Cell attachment site"
FT MOTIF 529..531
FT /note="Cell attachment site"
FT COMPBIAS 301..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1019 AA; 107984 MW; 66E4C334B83BBA21 CRC64;
MGLHDSFLAL LLLLGGAWAQ QAEINARVLR AQDCPVDLFF VLDTSESVAL RVKPFGDLVA
QVKDFTNRFI DKLTERYFRC DRFLAWNAGA LHYSDSVVII KDLTAMPSGR AELKNSVSAI
NYIGKGTHTD CAIKQGIERL LLGGSHLKEN KYLIVVTDGH PLEGYKEPCG GLDDAANEAK
HLGIKVFSVA ISPHHLDQRL NIIATDHAYR RNFTATSLKP TRDLDVEETI NNIIEMIKDN
MEQSCCSFEC HPPRGPPGPP GDPGHEGERG KPGLPGQKGD AGDPGRPGDM GPVGYQGMKG
DKGSRGEKGS RGAKGAKGEK GKRGIDGIDG MKGEAGYPGL PGCKGSPGFD GTQGPPGPKG
DPGAYGPKGG KGEPGEDGKP GRQGIPGSPG EKGAPGNRGE PGPLGETGDE GSPGADGPPG
ERGSNGERGP PGSPGDRGPR GDLGEPGPPG DQGREGPLGP PGDQGEPGPP GPKGYRGDDG
PRGNEGPKGS PGAPGLPGDP GLMGERGEDG PPGNGTIGFP GAPGQQGDRG DPGINGTKGY
VGPKGDEGEA GDPGNDNPTA GPSGIKGAKG HRGPEGRPGP PGPVGPPGPD ECEILDIIMK
MCSCCECTCG PVDLLFVLDS SESIGLQNFQ IAKDFIIKVI DRLSKDERVK FEPGESRVGV
VQYSHNNTQE LVAMGDANID NIGALKQAVK NLKWIAGGTH TGEALQFSKE NLLRRFTSNN
NVAIVITDGR SDTLRDRTPL TSLCEVTPVV SLGIGDIFRN NPNPDQLNDI ACLGMPRRQG
LSIQRDNYAE LLDDSFLQNI TSYVCREKKC PDYTCPITFA NPADIMLLVD SSTSVGSKNF
DTTKNFVKRL AERFLEASKP AEDSVRVSVV QYSGRNQQKV EVPFQRNYTV IAKAVDNMEF
MNEATDVNAA LQYIMGLYQR SSRSGAKKKV LVFSDGNSQG ITARAIERTV QEVQQAGIEV
YVLAVGSQVN EPNVRVLVTG KSTNYDVAYG ERHLFRVPDY TSLLRGVFYQ TVSRKIAVD
